Any feedback?
Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Homo sapiens and UniProt Accession Q16775
for references in articles please use BRENDA:EC3.1.2.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.2.6 hydroxyacylglutathione hydrolaseIUBMB Comments
Also hydrolyses S-acetoacetylglutathione, but more slowly.
Specify your search results
Word Map
- 3.1.2.6
- methylglyoxal
- gsh
- s-d-lactoylglutathione
-
glyoxalases
- d-lactate
-
glycation
-
glutathione-dependent
- dehydroascorbate
- monodehydroascorbate
- hemithioacetal
-
d-lactic
- mdhar
-
dicarbonyls
- trypanothione
- 2-oxoaldehydes
-
4.4.1.5
- lactoylglutathione
- metallo-beta-lactamase
- drug development
- biotechnology
- pharmacology
- medicine
- agriculture
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glyoxalase ii, glyoxalase 2, gly ii, glyii, glxii, glx2-2, gloii, hydroxyacylglutathione hydrolase, cgloii, glo ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoacetylglutathione hydrolase
Germ cell specific protein
GLO II
glyoxalase II
hydrolase, acetoacetylglutathione
hydrolase, hydroxyacylglutathione
Round spermatid protein RSP29
S-2-hydroxylacylglutathione hydrolase
additional information
enzyme is a member of the zinc metallohydrolase family with a beta-lactamase fold
acetoacetylglutathione hydrolase
-
-
-
-
Germ cell specific protein
-
-
-
-
GLO II
-
-
-
-
glyoxalase II
-
-
-
-
hydrolase, acetoacetylglutathione
-
-
-
-
hydrolase, hydroxyacylglutathione
-
-
-
-
Round spermatid protein RSP29
-
-
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
active site residue Tyr175 contributes to the binding of glutathione derivatives by its hydroxyl group which forms hydrogen binds to the glycine in the glutathione moiety
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY
9025-90-5
-
9025-92-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
?
slow model substrate for computational study, the substrate does not coordinate to any of the zinc ions in the Michaelis complex. The hydroxyl group forms a hydrogen bond to the Asp58 residue.
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
N-hydroxy-N-bromophenylcarbamate + glutathione
-
weak substrate
-
-
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
-
thioester hydrolysis promoted by a mononuclear zinc complex
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
S-D-lactoylglutathione
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
55.6% of the activity with S-lactoylglutathione
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
8.6% of the activity with S-lactoylglutathione
-
-
?
S-formylglutathione + H2O
formate + glutathione
-
37.7% of the activity with S-lactoylglutathione
-
-
?
S-glycerylglutathione + H2O
glycerate + glutathione
-
61.6% of the activity with S-lactoylglutathione
-
-
?
S-glycoloylglutathione + H2O
glycolate + glutathione
-
38.6% of the activity with S-lactoylglutathione
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
4.8% of the activity with S-lactoylglutathione
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
-
13.5% of the activity with S-lactoylglutathione
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
29.2% of the activity with S-lactoylglutathione
-
-
?
additional information
?
-
-
enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
-
?
additional information
?
-
enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
-
?
additional information
?
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
-
-
?
additional information
?
-
the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins
-
-
?
additional information
?
-
The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction.
-
-
?
additional information
?
-
-
the enzyme does not promote S-glutathionylation of GAPDH
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
additional information
?
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
-
-
?
additional information
?
-
the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins
-
-
?
additional information
?
-
The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction.
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
glyoxalase I is a binuclear zinc-enzyme, Zn2+ stabilizes the charge of tetrahedral intermediate thereby lowering the barrier for the nucleophilic attack, while Zn1 stabilizes the charge of the thiolate product, thereby facilitating the C-S bond cleavage
Zinc
-
the mononuclear zinc complex [(bpta)Zn](ClO4)2 x 0.5 H2O promotes the hydrolysis of thioester when dissolved in CH3CN:H2O (50:50 buffered at pH 9.0). This reaction results in the formation of a mixture of CD3SH and a zinc thiolate complex, the latter of which can be protonated to generate additional CD3SH
Zn2+
Zn2+
-
essential for maintainance of native structure of the enzyme. Binding to the apoenzyme occurs during an essential step of refolding
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acidic phospholipids
-
noncompetitive inhibition, lower thermal stability of the enzyme, inhibit protein intermolecular interactions/aggregation by thermal denaturation, small changes in the secondary structure are caused
-
cardiolipin
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
dioleoyl phosphatidic acid
-
i.e. DOPA, negatively charged phospholipid, strongly inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
dipalmitoylphosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
Guanidine-HCl
-
below 1 M, inactivation occurs without loss of the secondary structure
phosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
additional information
-
no effect by neutral phospholipids, phospholipid binding studies
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the mononuclear zinc complex [(bpta)Zn](ClO4)2 x 0.5 H2O promotes the hydrolysis of thioester when dissolved in CH3CN:H2O (50:50 buffered at pH 9.0). This reaction results in the formation of a mixture of CD3SH and a zinc thiolate complex, the latter of which can be protonated to generate additional CD3SH
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.152
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid
0.169
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of cardiolipin
0.191
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of dipalmitoylphosphatidylserine
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics in presence of liposomes consisting of different phospholipids
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
recombinant wild-type enzyme, pH 7.1, 37°C
0.035
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
recombinant mutant Y175F, pH 7.1, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytosolic and mitochondrial isozyme, both encoded by gene HAGH for hydroxyacylglutathione hydrolase
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transcription of glyoxalase II is about threefold increased in cancerous tissue comared to noncancerous tissue. Glyoxalase II activity is significantly lower in pathological tissues than in normal ones
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mitochondrial isozyme is targeted directly to the mitochondrial matrix due to a mitochondrial targeting sequence
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme limits lysine N-acetylation and N-succinylation of mitochondrial proteins
metabolism
the enzyme performs S-glutathionylation of actin and malate dehydrogenase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLO2_HUMAN
308
0
33806
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Computational study, the bond distances of the bridging hydroxide to the two zinc ions are calculated to be 1.99 and 1.95 A, to be compared to the crystallographic distances of 2.03 and 1.99 A. The computed Zn-Zn distance of 3.29 A is also in very good agreement with the crystallographic distance of 3.34 A.
glyoxalase II and its complex with S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W199F
-
mid-point of unfolding transition curve is not very different from that of wild-type. Stability of the active site is slightly affected
W57F
-
mid-point of unfolding transition curve is not very different from that of wild-type enzyme. Stability of the active site is slightly affected
Y175F
-
site-directed mutagenesis, mutation has a marginal effect on kcat, but leads to a 8fold increased Km for S-(2-hydroxyacyl)glutathione compared to the wild-type, mutant shows a 30fold increased sensitivity to inhibition by S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione compared to the wild-type enzyme
additional information
introduction of beta-lactamase activity into the alphabeta/betaalpha metallohydrolase scaffold of glyoxalase II. The resulting enzyme, evMBL8 (evolved metallo beta-lactamase 8), completely loses its original activity and, instead, catalyzes the hydrolysis of, thus increasing resistance to Escherichia coli growth on cefotaxime by a factor of about 100
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partially proteolyzed by trypsin, under nondenaturing conditions, only at the level of the C-terminal region. Inactivation of the enzyme without loss of the secondary structure
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis of the single HAGH gene encoding both the cytosolic and mitochondrial isozymes, in vitro transcription, 2 splicing forms of mRNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
cultivation of estrogen receptor positive MCF7 and estrogen receptor neagtive BT20 human breast cancer cells in presence of tamoxifen and 17beta-estradiol. Estradiol causes up to 60% decrease in enzyme mRNA in MCF7 cells, while there are no significant changes in presence of tamoxifen. In BT20 cells, tamoxifen causes a reduction of enzyme expression up to 85%.
medicine
GLX2 serves as a pro-survival factor of the p53 family and plays a critical role in the normal development and in the pathogenesis of various human diseases, including cancer, diabetes, and neurodegenerative diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
vander Jagt, D.L.
The glyoxalase system
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
597-641
1989
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
-
Uotila, L.
Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases
Biochemistry
12
3938-3943
1973
Homo sapiens
Uotila, L.
Glutathione thiol esterases of human red blood cells. Fractionation by gel electrophoresis and isoelectric focusing
Biochim. Biophys. Acta
580
277-288
1979
Homo sapiens
Uotila, L.
Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver
Biochemistry
12
3944-3951
1973
Homo sapiens
Van der Jagt, D.L.
Glyoxalase II: molecular characteristics, kinetic and mechanism
Biochem. Soc. Trans.
21
522-527
1993
Homo sapiens, Rattus norvegicus
Gillespie, E.
The tumor promoting phorbol diester, 12-O-tetradecanoylphorbol-13-acetate (TPA) increases glyoxalase I and decreases glyoxalase II activity in human polymorphonuclear leukocytes
Biochem. Biophys. Res. Commun.
98
463-470
1981
Homo sapiens
Cameron, A.D.; Ridderstrom, M.; Olin, B.; Mannervik, B.
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
Structure Fold. Des.
7
1067-1078
1999
Homo sapiens
Aceto, A.; Dragani, B.; Melino, S.; Principato, G.; Saccucci, F.; Gualtieri, G.; Petruzzelli, R.
Structural characterization of human glyoxalase II as probed by limited proteolysis
Biochem. Mol. Biol. Int.
44
761-769
1998
Homo sapiens
Allen, R.E.; Lo, T.W.C.; Thornalley, P.J.
Purification and characterisation of glyoxalase II from human red blood cells
Eur. J. Biochem.
213
1261-1267
1993
Homo sapiens
Uotila, L.
Glutathione thiol esterases
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
767-804
1989
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus
-
Dragani, B.; Cocco, R.; Ridderstroem, M.; Stenberg, G.; Mannervik, B.; Aceto, A.
Unfolding and refolding of human glyoxalase II and its single-tryptophan mutants
J. Mol. Biol.
291
481-490
1999
Homo sapiens
Ridderstrm, M.; Saccucci, F.; Hellman, U.; Bergman, T.; Principato, G.; Mannervik, B.
Molecular cloning, heterologous expression, and characterization of human glyoxalase II
J. Biol. Chem.
271
319-323
1996
Homo sapiens (Q16775), Homo sapiens
Ridderstroem, M.; Jemth, P.; Cameron, A.D.; Mannervik, B.
The active-site residue tyr-175 in human glyoxalase II contributes to binding of glutathione derivatives
Biochim. Biophys. Acta
1481
344-348
2000
Homo sapiens
Cordell, P.A.; Futers, T.S.; Grant, P.J.; Pease, R.J.
The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II
J. Biol. Chem.
279
28653-28661
2004
Homo sapiens, Homo sapiens (Q16775)
Scire, A.; Tanfani, F.; Saccucci, F.; Bertoli, E.; Principato, G.
Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only
Proteins
41
33-39
2000
Bos taurus, Homo sapiens
Scire, A.; Saccucci, F.; Bertoli, E.; Cambria, M.T.; Principato, G.; D'Auria, S.; Tanfani, F.
Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II
Proteins
48
126-133
2002
Homo sapiens
Rulli, A.; Antognelli, C.; Prezzi, E.; Baldracchini, F.; Piva, F.; Giovannini, E.; Talesa, V.
A possible regulatory role of 17beta-estradiol and tamoxifen on glyoxalase I and glyoxalase II genes expression in MCF7 and BT20 human breast cancer cells
Breast Cancer Res. Treat.
96
187-196
2006
Homo sapiens (Q16775), Homo sapiens
Antognelli, C.; Baldracchini, F.; Talesa, V.N.; Costantini, E.; Zucchi, A.; Mearini, E.
Overexpression of glyoxalase system enzymes in human kidney tumor
Cancer J.
12
222-228
2006
Homo sapiens
Xu, Y.; Chen, X.
Glyoxalase II, a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73, is a pro-survival factor of the p53 family
J. Biol. Chem.
281
26702-26713
2006
Homo sapiens (Q16775), Homo sapiens
Park, H.; Nam, S.; Lee, J.K.; Yoon, C.N.; Mannervik, B.; Benkovic, S.J.; Kim, H.
Design and evolution of new catalytic activity with an existing protein scaffold
Science
311
535-538
2006
Homo sapiens (Q16775)
Chen, S.L.; Fang, W.H.; Himo, F.
Reaction mechanism of the binuclear zinc enzyme glyoxalase II - A theoretical study
J. Inorg. Biochem.
103
274-281
2009
Homo sapiens (Q16775)
Danford, J.J.; Arif, A.M.; Berreau, L.M.
Thioester hydrolysis promoted by a mononuclear zinc complex
Inorg. Chem.
49
778-780
2010
Homo sapiens
Ercolani, L.; Scire, A.; Galeazzi, R.; Massaccesi, L.; Cianfruglia, L.; Amici, A.; Piva, F.; Urbanelli, L.; Emiliani, C.; Principato, G.; Armeni, T.
A possible S-glutathionylation of specific proteins by glyoxalase II An in vitro and in silico study
Cell Biochem. Funct.
34
620-627
2016
Homo sapiens (Q16775)
James, A.M.; Hoogewijs, K.; Logan, A.; Hall, A.R.; Ding, S.; Fearnley, I.M.; Murphy, M.P.
Non-enzymatic N-acetylation of lysine residues by acetylCoA often occurs via a proximal S-acetylated thiol intermediate sensitive to glyoxalase II
Cell Rep.
18
2105-2112
2017
Homo sapiens (Q16775)
EXTERNAL LINKS (specific for EC-Number 3.1.2.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
